1. CHAPTER 11 CELL COMMUNICATION Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Section B: Signal Reception and the Initiation of Transduction 1.A signal molecule binds to a receptor protein, causing the protein to change shape 2. Most signal receptors are plasma membrane proteins

2. A cell targeted by a particular chemical signal has a receptor protein that recognizes the signal molecule. Recognition occurs when the signal binds to a specific site on the receptor because it is complementary in shape. When ligands (small molecules that bind specifically to a larger molecule) attach to the receptor protein, the receptor typically undergoes a change in shape. This may activate the receptor so that it can interact with other molecules. For other receptors this leads to aggregation of receptors. 1. A signal molecule binds to a receptor protein causing the protein to change shape Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

3. Most signal molecules are water-soluble and too large to pass through the plasma membrane. They influence cell activities by binding to receptor proteins on the plasma membrane. Binding leads to change in the shape or the receptor or to aggregation of receptors. These trigger changes in the intracellular environment. Three major types of receptors are G-protein-linked receptors, tyrosine-kinase receptors, and ion-channel receptors. 2. Most signal receptors are plasma membrane proteins Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

4. A G-protein-linked receptor consists of a receptor protein associated with a G-protein on the cytoplasmic side. The receptor consists of seven alpha helices spanning the membrane. Effective signal molecules include yeast mating factors, epinephrine, other hormones, and neurotransmitters. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.6

5. The G protein acts as an on-off switch. If GDP is bound, the G protein is inactive. If ATP is bound, the G protein is active. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.7a

6. The G-protein system cycles between on and off. When a G-protein-linked receptor is activated by binding with an extracellular signal molecule, the receptor binds to an inactive G protein in membrane. This leads the G protein to substitute GTP for GDP. The G protein then binds with another membrane protein, often an enzyme, altering its activity and leading to a cellular response. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.7b

7. The G protein can also act as a GTPase enzyme and hydrolyzes the GTP, which activated it, to GDP. This change turns the G protein off. The whole system can be shut down quickly when the extracellular signal molecule is no longer present. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.7c

8. G-protein receptor systems are extremely widespread and diverse in their functions. In addition to functions already mentioned, they play an important role during embryonic development and sensory systems. Similarities among G proteins and G-protein- linked receptors suggest that this signaling system evolved very early. Several human diseases are the results of activities, including bacterial infections, that interfere with G-protein function. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

9. The tyrosine-kinase receptor system is especially effective when the cell needs to regulate and coordinate a variety of activities and trigger several signal pathways at once. Extracellular growth factors often bind to tyrosine- kinase receptors. The cytoplasmic side of these receptors function as a tyrosine kinase, transferring a phosphate group from ATP to tyrosine on a substrate protein. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

10. A individual tyrosine-kinase receptors consists of several parts: an extracellular signal-binding sites, a single alpha helix spanning the membrane, and an intracellular tail with several tyrosines. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.8a

11. When ligands bind to two receptors polypeptides, the polypeptides aggregate, forming a dimer. This activates the tyrosine-kinase section of both. These add phosphates to the tyrosine tails of the other polypeptide. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.8b

12. The fully-activated receptor proteins activate a variety of specific relay proteins that bind to specific phosphorylated tyrosine molecules. One tyrosine-kinase receptor dimer may activate ten or more different intracellular proteins simultaneously. These activated relay proteins trigger many different transduction pathways and responses. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.8b

13. Ligand-gated ion channels are protein pores that open or close in response to a chemical signal. This allows or blocks ion flow, such as Na + or Ca 2+. Binding by a ligand to the extracellular side changes the protein’s shape and opens the channel. Ion flow changes the concentration inside the cell. When the ligand dissociates, the channel closes. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

14. Ligand-gated ion channels are very important in the nervous system. Similar gated ion channels respond to electrical signals. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

15. Other signal receptors are dissolved in the cytosol or nucleus of target cells. The signals pass through the plasma membrane. These chemical messengers include the hydrophobic steroid and thyroid hormones of animals. Also in this group is nitric oxide (NO), a gas whose small size allows it to slide between membrane phospholipids. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

16. Testosterone, like other hormones, travels through the blood and enters cells throughout the body. In the cytosol, they bind and activate receptor proteins. These activated proteins enter the nucleus and turn on genes that control male sex characteristics. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 11.10

17. These activated proteins act as transcription factors. Transcription factors control which genes are turned on - that is, which genes are transcribed into messenger RNA (mRNA). The mRNA molecules leave the nucleus and carry information that directs the synthesis (translation) of specific proteins at the ribosome. Other intracellular receptors are already in the nucleus and bind to the signal molecules there (e.g., estrogen receptors). Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings